A
Atanu Singha Roy
Researcher at National Institute of Technology, Meghalaya
Publications - 59
Citations - 1520
Atanu Singha Roy is an academic researcher from National Institute of Technology, Meghalaya. The author has contributed to research in topics: Human serum albumin & Chemistry. The author has an hindex of 19, co-authored 48 publications receiving 1071 citations. Previous affiliations of Atanu Singha Roy include Indian Institute of Technology Kharagpur & Lovely Professional University.
Papers
More filters
Journal ArticleDOI
An investigation into the identification of potential inhibitors of SARS-CoV-2 main protease using molecular docking study.
TL;DR: Rutin ( a natural compound) has the highest inhibitor efficiency among the 33 molecules studied, followed by ritonavir (control drug), emetine (anti-protozoal), hesperidin (a natural compound), lopinavir ( control drug) and indinavir(anti-viral drug).
Journal ArticleDOI
Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins
Durba Roy,Samrajnee Dutta,Shyam Sundar Maity,Sanjib Ghosh,Atanu Singha Roy,Kalyan Sundar Ghosh,Swagata Dasgupta +6 more
TL;DR: The steady-state fluorescence studies and FTIR spectra suggest that in both the albumins, C and EC stabilize the α-helix at the cost of a corresponding loss in the β-sheet structure.
Journal ArticleDOI
Molecular recognition of bio-active flavonoids quercetin and rutin by bovine hemoglobin: an overview of the binding mechanism, thermodynamics and structural aspects through multi-spectroscopic and molecular dynamics simulation studies.
TL;DR: Investigation of the binding of two bio-active flavonoids with bovine hemoglobin established that these flavonoid are efficient in the inhibition of glucose mediated glycation of BHb.
Journal ArticleDOI
A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin
TL;DR: The interaction of naringin with bovine serum albumin has been performed using fluorescence, circular dichroism and fourier transform infrared spectroscopy in 20 mM phosphate buffer of pH 7.0 as well as molecular docking studies, indicating that the interaction occurred mainly through hydrophobic interactions.
Journal ArticleDOI
Exploring the interaction of bioactive kaempferol with serum albumin, lysozyme and hemoglobin: A biophysical investigation using multi-spectroscopic, docking and molecular dynamics simulation studies.
Sourav Das,Zaved Hazarika,Sharat Sarmah,Kakali Baruah,Mostofa Ataur Rohman,Debojit Paul,Anupam Nath Jha,Atanu Singha Roy +7 more
TL;DR: The ligand, KMP was able to quench the intrinsic fluorescence of these three proteins efficiently through static quenching mode and alter the micro-environment near the Trp fluorophore of the proteins.